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secretion of macrophage-colony stimulation factor(67) as well as the degradation of
proteins by monocytic cells (68).
Methylglyoxal toxicity appears to be related to its effect on cell growth as well.
The addition of exogenous methylglyoxal to cell cultures is known to inhibit growth, a
consequence that can be reversed by the removal of the ketoaldehyde (69). This effect
was found to be directly associated with the inhibition of protein synthesis (28), primarily
during the S and G2 phases of the cell cycle (70). Further testing suggests that the effect
was not due to any direct interaction with DNA (70) or mRNA (58). Anecdotal evidence
have led to the proposal that the inhibition of protein synthesis may be due to the
inactivation of either tRNA or ribosomal proteins due to formation of arginyl /
methylglyoxal adducts (71).
Much evidence suggests that methylglyoxal can cause damaging effects upon
living organisms; however, the efficiency of the glyoxalase system is thought to maintain
toxic o-ketoaldehydes at levels below physiological relevance. It is therefore probable
that only when an inhibited or impaired glyoxalase system allows chronic levels of
methylglyoxal to be sustained that damage may follow.
1.6 S-D-lactoylglutathione
The product of GLO-1 activity with the methylglyoxal derived hemithioacetal
produces a high-energy intermediate, SLG. Due to its poor membrane permeability, this
intermediate is thought to be produced and metabolized only in the cytosol of the cell
(24). Physiological levels of SLG are generally found to be in the micromolar range with12
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Gillis, Glen S. Nucleotide Inhibition of Glyoxalase II, dissertation, May 1999; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc2183/m1/21/: accessed March 29, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .